Abstract
Dynamics of hydration water is essential for the function of biomacromolecules. Previous studies have demonstrated that water molecules exhibit subdiffusion on the surface of biomacromolecules; yet the microscopic mechanism remains vague. Here, by performing neutron scattering, molecular dynamics simulations, and analytic modeling on hydrated perdeuterated protein powders, we found water molecules jump randomly between trapping sites on protein surfaces, whose waiting times obey a broad distribution, resulting in subdiffusion. Moreover, the subdiffusive exponent gradually increases with observation time towards normal diffusion due to a many-body volume-exclusion effect.
- Received 24 November 2017
- Revised 12 March 2018
DOI:https://doi.org/10.1103/PhysRevLett.120.248101
© 2018 American Physical Society
Physics Subject Headings (PhySH)
Viewpoint
The Dance of Water Molecules around Proteins
Published 11 June 2018
A combination of experiments, simulations, and modeling has revealed the anomalous diffusion of water molecules along the surfaces of proteins.
See more in Physics